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Literature summary for 1.14.99.29 extracted from

  • Cano, V.; Medrano, F.; Park, M.; Valentini, S.
    Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site (2010), Amino Acids, 38, 479-490.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene LIA1, expression in Escherichia coli strain BL21(DE3) as GST-tagged protein Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E113A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
E116A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
E116D site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
E238A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
E271A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
E80A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
H112A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
H237A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
H270A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae
H79A site-directed mutagenesis, the mutant is completely inactive in deoxyhypusine hydroxylation, structure comparison to the wild-type enzyme Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required, essential structural role for iron binding in addition to its contribution to the catalysis of hypusine formation in the eIF-5A precursor. Lia1 is an iron metalloenzyme. Determination of metal contents in purified enzyme samples, overview. The apoenzyme has a larger hydrodynamic size than the holoenzyme Saccharomyces cerevisiae
additional information Lia1 contains no cadmium, cobalt, chromium, copper, magnesium, manganese, nickel and zinc Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
The apoenzyme has a larger hydrodynamic size than the holoenzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 Saccharomyces cerevisiae activation of eIF5A eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
additional information Saccharomyces cerevisiae Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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gene YJR070C or LIA1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged Lia1 from Escherichia coli strain BL21(DE3) by two steps of glutathione affinity chromatography and gel filtration. Separation of iron-free and iron-bound forms by gel filtration and native electrophoresis Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2
-
Saccharomyces cerevisiae eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
eIF5A-N6-(4-aminobutyl)-L-lysine + AH2 + O2 activation of eIF5A Saccharomyces cerevisiae eIF5A-N6-(4-amino-2-hydroxybutyl)-L-lysine + A + H2O
-
?
additional information Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
More ability of Lia1 to undergo conformational changes, the active enzyme occurs in a stabilized and compact three-dimensional fold with bound metal. Loss of tertiary contacts upon iron displacement led to an elongated conformation of Lia1, in which the N- and C-terminal domains are no longer in close proximity to guarantee the proper orientation of the active groups within the active site pocket. Lia1 contains HEAT-like repeats with a role for mediating protein-protein interactions. Structure spectral analysis of iron-free and iron-bound enzyme, and effects of pH on Lia1 catalytic activity and tertiary structure, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
deoxyhypusine hydroxylase
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Saccharomyces cerevisiae
Lia1
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
metabolism the unique amino acid hypusine is formed exclusively in eIF5A by the successive action of deoxyhypusine synthase and deoxyhypusine hydroxylase Saccharomyces cerevisiae
physiological function the enzyme activates eIF5A, that plays a role in the elongation step of translation Saccharomyces cerevisiae